1up6: Difference between revisions

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[[Image:1up6.~~jpg~~|left|200px]]

[[Image:1up6.png|left|200px]]

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~~'''~~STRUCTURE OF THE 6-PHOSPHO-BETA GLUCOSIDASE FROM THERMOTOGA MARITIMA AT 2.55 ANGSTROM RESOLUTION IN THE TETRAGONAL FORM WITH MANGANESE, NAD+ AND GLUCOSE-6-PHOSPHATE~~'''~~

===STRUCTURE OF THE 6-PHOSPHO-BETA GLUCOSIDASE FROM THERMOTOGA MARITIMA AT 2.55 ANGSTROM RESOLUTION IN THE TETRAGONAL FORM WITH MANGANESE, NAD+ AND GLUCOSE-6-PHOSPHATE===

~~==Overview==~~

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~~Among the numerous well-characterized families of glycosidases~~, ~~family 4 appears to be the anomaly~~, ~~requiring both catalytic NAD+ and a divalent metal for activity. The unusual cofactor requirement prompted~~ the ~~proposal of a mechanism involving key NAD+-mediated redox steps as well as elimination of~~ the ~~glycosidic oxygen. Primary kinetic isotope effects for the 2- and 3-deutero substrate analogues, isotopic exchange with solvent, and structural analysis of a 6-phospho-beta-glucosidase, BglT~~ (~~E.C. 3.2~~.1.6), ~~provided evidence in support of~~ the ~~proposed mechanism, which has striking resemblances to that of the sugar dehydratases. Furthermore, analysis of the stereochemical outcome indicated that family 4 enzymes are retaining glycosidases~~.

The line below this paragraph, {{ABSTRACT_PUBMED_15237973}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15237973 is the PubMed ID number.

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==About this Structure==

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[[Category: Family4 hydrolase]]

[[Category: Nad dependent]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 11~~:31:34 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:40:33 2008''

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-[[Image:1up6.jpg|left|200px]]
+{{Seed}}
+[[Image:1up6.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1up6|  PDB=1up6  |  SCENE=  }}
-'''STRUCTURE OF THE 6-PHOSPHO-BETA GLUCOSIDASE FROM THERMOTOGA MARITIMA AT 2.55 ANGSTROM RESOLUTION IN THE TETRAGONAL FORM WITH MANGANESE, NAD+ AND GLUCOSE-6-PHOSPHATE'''
+===STRUCTURE OF THE 6-PHOSPHO-BETA GLUCOSIDASE FROM THERMOTOGA MARITIMA AT 2.55 ANGSTROM RESOLUTION IN THE TETRAGONAL FORM WITH MANGANESE, NAD+ AND GLUCOSE-6-PHOSPHATE===
-==Overview==
+<!--
-Among the numerous well-characterized families of glycosidases, family 4 appears to be the anomaly, requiring both catalytic NAD+ and a divalent metal for activity. The unusual cofactor requirement prompted the proposal of a mechanism involving key NAD+-mediated redox steps as well as elimination of the glycosidic oxygen. Primary kinetic isotope effects for the 2- and 3-deutero substrate analogues, isotopic exchange with solvent, and structural analysis of a 6-phospho-beta-glucosidase, BglT (E.C. 3.2.1.6), provided evidence in support of the proposed mechanism, which has striking resemblances to that of the sugar dehydratases. Furthermore, analysis of the stereochemical outcome indicated that family 4 enzymes are retaining glycosidases.
+The line below this paragraph, {{ABSTRACT_PUBMED_15237973}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15237973 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15237973}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Family4 hydrolase]]
 [[Category: Nad dependent]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:31:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:40:33 2008''